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PDBsum entry 3ltg
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protein Protein-protein interface(s) links
Transferase/transferase regulator PDB id
3ltg

 

 

 

 

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Contents
Protein chains
522 a.a. *
51 a.a. *
* Residue conservation analysis
PDB id:
3ltg
Name: Transferase/transferase regulator
Title: Crystal structure of the drosophila epidermal growth factor receptor ectodomain complexed with a low affinity spitz mutant
Structure: Epidermal growth factor receptor. Chain: a, c. Fragment: ectodomain, residues 100-688. Synonym: gurken receptor, protein torpedo, drosophila relative of erbb. Engineered: yes. Protein spitz. Chain: d. Fragment: egf domain, residues 76-127.
Source: Drosophila melanogaster. Organism_taxid: 7227. Gene: torpedo. Degfr. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Gene: spitz. Expressed in: drosophila melanogaster. Expression_system_taxid: 7227. Expression_system_cell_line: schneider 2(s2) cells.
Resolution:
3.40Å     R-factor:   0.408     R-free:   0.427
Authors: D.Alvarado,D.E.Klein,M.A.Lemmon
Key ref: D.Alvarado et al. (2010). Structural basis for negative cooperativity in growth factor binding to an EGF receptor. Cell, 142, 568-579. PubMed id: 20723758
Date:
15-Feb-10     Release date:   25-Aug-10    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P04412  (EGFR_DROME) -  Epidermal growth factor receptor from Drosophila melanogaster
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		1426 a.a.
522 a.a.*
Protein chain
Pfam   ArchSchema ?
Q01083  (SPITZ_DROME) -  Protein spitz from Drosophila melanogaster
Seq:
Struc: 		234 a.a.
51 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 10 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chains A, C: E.C.2.7.10.1  - receptor protein-tyrosine kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H+
L-tyrosyl-[protein]
 + ATP
 = O-phospho-L-tyrosyl-[protein]
 + ADP
 + H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
Cell 142:568-579 (2010)
PubMed id: 20723758  
 
 
Structural basis for negative cooperativity in growth factor binding to an EGF receptor.
D.Alvarado, D.E.Klein, M.A.Lemmon.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
22218287 N.J.Bessman, and M.A.Lemmon (2012).
Finding the missing links in EGFR.
  Nat Struct Mol Biol, 19, 1-3.  
21532939 D.J.Riese (2011).
Ligand-based receptor tyrosine kinase partial agonists: New paradigm for cancer drug discovery?
  Expert Opin Drug Discov, 6, 185-193.  
21264347 J.A.Krall, E.M.Beyer, and G.MacBeath (2011).
High- and low-affinity epidermal growth factor receptor-ligand interactions activate distinct signaling pathways.
  PLoS One, 6, e15945.  
21316780 P.Vanhee, A.M.van der Sloot, E.Verschueren, L.Serrano, F.Rousseau, and J.Schymkowitz (2011).
Computational design of peptide ligands.
  Trends Biotechnol, 29, 231-239.  
22020299 S.T.Low-Nam, K.A.Lidke, P.J.Cutler, R.C.Roovers, P.M.van Bergen en Henegouwen, B.S.Wilson, and D.S.Lidke (2011).
ErbB1 dimerization is promoted by domain co-confinement and stabilized by ligand binding.
  Nat Struct Mol Biol, 18, 1244-1249.  
20946975 B.Z.Shilo (2010).
Insider influence on ErbB activity.
  Cell, 143, 181-182.  
20723751 D.J.Leahy (2010).
The ins and outs of EGFR asymmetry.
  Cell, 142, 513-515.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.

 

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